A generic cross-seeding approach to protein crystallization
© Ido Caspy et al. 2025.
| Publié dans: | Journal of applied crystallography. - 1998. - 58(2025), Pt 2 vom: 01. Apr., Seite 383-391 |
|---|---|
| Auteur principal: | |
| Autres auteurs: | , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2025
|
| Accès à la collection: | Journal of applied crystallography |
| Sujets: | Journal Article X-ray crystallography cross-seeding macromolecular crystallization nucleation protein crystals |
| Résumé: | © Ido Caspy et al. 2025. Obtaining diffraction-quality crystals is often the rate-limiting step during structure determination of biological macromolecules by X-ray crystallography. To address this problem, we investigated a cross-seeding approach with a mixture integrating a heterogeneous set of protein crystal fragments to be used as generic seeds. The fragments are nanometre-sized templates chosen to promote crystal nucleation of protein samples unrelated to the proteins forming the seeds. An atypical crystal form of the human serine hydrolase retinoblastoma binding protein 9 was obtained by adding the mixture to the protein sample before performing standard crystallization assays. The structure was solved by X-ray crystallography at 1.4 Å resolution. Follow-up experiments showed that crystal fragments of α-amylase were critical components in this particular result. The limitations and future applications of our experimental developments are discussed |
|---|---|
| Description: | Date Revised 03.04.2025 published: Electronic-eCollection Citation Status PubMed-not-MEDLINE |
| ISSN: | 0021-8898 |
| DOI: | 10.1107/S1600576725000457 |